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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

UniprotKB/SwissProt ID: PP1G_HUMAN (P36873)

Gene Name: PPP1CC

Organism: Homo sapiens (Human).

Function: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density- associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus, nucleoplasm. Nucleus speckle. Chromosome, centromere, kinetochore. Cleavage furrow. Midbody. Mitochondrion. Note=Colocalizes with SPZ1 in the nucleus (By similarity). Colocalizes with URI1 at mitochondrion

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Network with metabolic pathway:
Kegg map ID Pathway Link
map04720Long-term potentiation
map04728Dopaminergic synapse
map05031Amphetamine addiction
map03015mRNA surveillance pathway
map04114Oocyte meiosis
map04270Vascular smooth muscle contraction
map04510Focal adhesion
map04810Regulation of actin cytoskeleton
map04910Insulin signaling pathway
map05034Alcoholism
map05168Herpes simplex infection
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR004843
IPR006186

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1IT6 X-ray 2.00 A A/B1-323Link
1JK7 X-ray 1.90 A A1-323Link
1U32 X-ray 2.00 A A6-298Link
2BCD X-ray 2.10 A A1-323Link
2BDX X-ray 2.30 A A1-323Link

The S-nitrosylation sites of PP1G_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1127NFFLLRGNHE C ASINRIYGFY EEEEEECCCH H HHHHHHHHHH 2.53%HC0319483679in vivo
2155NIKLWKTFTD C FNCLPIAAIV CHHHHHHHHH H HHHHHHHHHH 2.10%HC0719483679in vivo
3158LWKTFTDCFN C LPIAAIVDEK HHHHHHHHHH H HHHHHHHCCC 2.10%HC0719483679in vivo
4245FLHKHDLDLI C RAHQVVEDGY HHHHCCCCEE E HHHHHHHHHH 4.01%HC0119483679in vivo